1SRR

CRYSTAL STRUCTURE OF A PHOSPHATASE RESISTANT MUTANT OF SPORULATION RESPONSE REGULATOR SPO0F FROM BACILLUS SUBTILIS

Summary for 1SRR

• Entry DOI: 10.2210/pdb1srr/pdb
• Descriptor: SPORULATION RESPONSE REGULATORY PROTEIN, CALCIUM ION (3 entities in total)
• Functional Keywords: aspartate pocket, sporulation response regulator, two component system, regulatory protein
• Biological source: Bacillus subtilis
• Cellular location: Cytoplasm (Probable): P06628
• Total number of polymer chains: 3
• Total formula weight: 42585.85

Authors

Madhusudan,Whiteley, J.M.,Hoch, J.A.,Zapf, J.,Xuong, N.H.,Varughese, K.I. (deposition date: 1996-04-10, release date: 1997-04-21, Last modification date: 2024-02-14)

Primary citation

Madhusudan,Zapf, J.,Whiteley, J.M.,Hoch, J.A.,Xuong, N.H.,Varughese, K.I.
Crystal structure of a phosphatase-resistant mutant of sporulation response regulator Spo0F from Bacillus subtilis.
Structure, 4:679-690, 1996

PubMed Abstract: Spo0F, a phosphotransferase containing an aspartyl pocket, is involved in the signaling pathway (phosphorelay) controlling sporulation in Bacillus subtilis. It belongs to the superfamily of bacterial response regulatory proteins, which are activated upon phosphorylation of an invariant aspartate residue. This phosphorylation is carried out in a divalent cation dependent reaction catalyzed by cognate histidine kinases. Knowledge of the Spo0F structure would provide valuable information that would enable the elucidation of its function as a secondary messenger in a system in which a phosphate is donated from Spo0F to Spo0B, the third of four main proteins that constitute the phosphorelay.

PubMed: 8805550
DOI: 10.1016/S0969-2126(96)00074-3

Experimental method

X-RAY DIFFRACTION (1.9 Å)